The crystal structure of the snake long α‐neurotoxin, α‐cobratoxin, bound to the pentameric
acetylcholine‐binding protein (AChBP) from Lymnaea stagnalis, was solved from good
quality density maps despite a 4.2 Å overall resolution. The structure unambiguously reveals
the positions and orientations of all five three‐fingered toxin molecules inserted at the
AChBP subunit interfaces and the conformational changes associated with toxin binding.
AChBP loops C and F that border the ligand‐binding pocket move markedly from their …

Two mistakes have been missed at the proof stage: Page 1516, section 'Detailed view of the
Cbtx–AChBP complex interface', the sentence starting line 18 should read 'In addition, Cbtx
Trp25, Asp27, Ala28, and Ile32 that surround the tip of loop II are within contact distance of
Tyr185 in AChBP subunit A and of Glu163, Gln55, Leu112, Met114, and Tyr164 in subunit
B'. Page 1519, section 'Reliability and implications of the Cbtx–AChBP complex structure',
the last sentence should read 'Mutation Tyr53Trp enhanced Bgtx affinity while mutation …